Reviewed, UniProtKB/Swiss-Prot Q57C76 (MURD_BRUAB)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoylalanine--D-glutamate ligase
    EC=6.3.2.9
Alternative name(s):
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
    D-glutamic acid-adding enzyme

Gene names

Name:	murD
Ordered Locus Names:	BruAb1_1428

Organism

Brucella abortus [Complete proteome] [HAMAP]

Taxonomic identifier

235 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) By similarity. HAMAP MF_00639
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP MF_00639
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639
Subcellular location	Cytoplasm By similarity HAMAP MF_00639.
Sequence similarities	Belongs to the murCDEF family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW folic acid and derivative biosynthetic process Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP UDP-N-acetylmuramoylalanine-D-glutamate ligase activity Inferred from electronic annotation. Source: HAMAP tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108981
Regions
	Nucleotide binding	121 – 127	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q57C76-1 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 460D244D6D7849CA	FASTA	467	48,694
	10 20 30 40 50 60 MIPITALKDK TVALFGLGGS GIATAKAIVA GGARIIAWDD NPDSVARAQS AGIATGDLRQ 70 80 90 100 110 120 ADWSQFAVFV LSPGVPLTHP QPHWSVDLAR AAGVEIIGDV ELFVRERNHI APDCPFIAIT 130 140 150 160 170 180 GTNGKSTTTA LIAHIIKATG RDMQLGGNIG TAILTLEPPC ADRFYVVECS SYQIDLAPSL 190 200 210 220 230 240 NPTAGILLNL TPDHLDRHGS MENYAAIKER LVAASGTAII GIDDAYCQAI ADRLHGAGIR 250 260 270 280 290 300 VVRISKEKHL DRGYFADGAK LLWAQDGEID EIASLEGIGS LRGAHNAQNA LAAIVACLSA 310 320 330 340 350 360 GLSLEEIHAG LKSFPGLAHR MEQVGRRGKV LFVNDSKATN AEATAPALSS FPQNIYWIVG 370 380 390 400 410 420 GVPKAGGINS LTAFFPRVAK AYLIGEAAAQ FAATLGGAVP FEISDTLAAA VAHAAGDAGN 430 440 450 460 DAAPEPVVLL SPACASFDQF QNFEKRGDAF RDAVLALPGV MPMRGGS

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74758.1.
RefSeq	YP_222119.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3339786.
GenomeReviews	Gene locus BruAb1_1428 in contig AE017223_GR.
KEGG	bmb:BruAb1_1428.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG750024.
OMA	VKYYNDS.
PhylomeDB	Q57C76.
Enzyme and pathway databases
BioCyc	BABO262698:BRUAB1_1428-MONOMER.
BRENDA	6.3.2.9. 575.
Family and domain databases
HAMAP	MF_00639. MurD. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR016040. NAD(P)-bd_dom. IPR005762. UDP-N-AcMur-Glu_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01087. murD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_BRUAB

Accession

Primary (citable) accession number: Q57C76

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	May 10, 2005
Last modified:	February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)